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Fosforilación Oxidativa
Dr. Dante Miranda Wilson
ADAPTACIONES EVOLUTIVAS ANTE
LA APARICION DEL OXÍGENO
ANAEROBIOS
FOSFORILACIÓN
OXIDATIVA
El ser humano vive porque es capaz de realizar
múltiples reacciones químicas, reguladas e
integradas a una velocidad compatible con la
máxima sobrevida en condiciones fisiológicas
Poder Reductor
Respiración Celular
Poder reductor:
Electrones con un alto potencial de transferencia
• Lugar: Mitocondria
FADH2
Complejo II
(succinato deshidrogenasa)
Citocromo
Complejo III reductasa
Complejo IV
Componentes de la cadena transportadora de electrones mitocondrial
Oxidant or reductant
Enzyme complex Mass (kd) Subunits Prosthetic group Matrix side Membrane Cytosolic side
core
NADH-Q 880 7* 34 FMN NADH Q
oxidoreductase
Fe-S
Succinate-Q 140 0* 4 FAD Succinate Q
reductase
Fe-S
Q-cytochrome c 250 1* 10 Heme bH Q Cytochrome c
oxidoreductase
Heme bL
Heme c1
Fe-S
Cytochrome c 160 3* 10 Heme a Cytochrome c
oxidase
Heme a3
CuA and CuB
Sources: J. W. DePierre and L. Ernster, Annu. Rev. Biochem. 46(1977):215; Y. Hatefi, Annu Rev. Biochem. 54(1985);1015;
and J. E. Walker, Q. Rev. Biophys. 25(1992):253.
*: Subunidades codificadas por DNA mitocondrial
NADH
FMN en Complejo I
FMN
Centros Fe-S
Fe+3 + e- Fe+2
FMN en Complejo I
Fe+3 + e- Fe+2
Coenzima Q
Coenzima Q
Citocromo reductasa
2 3
1 AcilCoA
Glicerol-3P
FAD
G3PDH(FAD)
Succinato Fumarato ETF (FAD)
FADH2
Oxido
Reductasa (Fe-S)
FAD UQ/UQH2
Fe-S
Hem b
Succinato
Deshidrogenasa
Complejo III
Citocromo
Reductasa
Citocromo
QH2
Fe+2-Cit c
Citocromo
Oxidasa
Citocromo Oxidasa (grupos Hem y Cu)
Citocromo c es una estructura altamente conservada:
Enz:ADP + Pi Enz:ATP
Esto indicaba que la síntesis de ATP por F1 no requería energía y que el
movimiento de protones serviría para liberar el ATP sintetizado.
Complejo V: ATP Sintasa
F1: αβγδε
(α3,β3,γ,δ,ε)
Fo: a,b,c
Matriz mitocondrial
Movimiento de protones a través de subunidad c de complejo Fo
Evidencia experimental que demuestra la rotación de subunidades
Gamma.
CIV: 4 H+ /4e H+ /e
Malato/α-cetoglutarato
antiporter
Transportadores mitocondriales
Reaction sequence ATP yield per glucose molecule
Glycolysis: Conversion of glucose into pyruvate (in the cytosol)
Phosphorylation of glucose -1
Phosphorylation of fructose 6-phosphate -1
Dephosphorylation of 2 molecules of 1,3-BPG +2
Dephosphorylation of 2 molecules of phosphoenolpyruvate +2
2 molecules of NADH are formed in the oxidation of 2 molecules of glyceraldehyde 3-phosphate
6 molecules of NADH are formed in the oxidation of 2 molecules each of isocitrate, α-ketoglutarate, and
malate
2 molecules of FADH2 are formed in the oxidation of 2 molecules of succinate
2 molecules of NADH formed in glycolysis; each yields 1.5 molecules of ATP (assuming transport of NADH +3
by the glycerol 3-phosphate shuttle)
2 molecules of NADH formed in the oxidative decarboxylation of pyruvate; each yields 2.5 molecules of +5
ATP
2 molecules of FADH2 formed in the citric acid cycle; each yields 1.5 molecules of ATP +3
6 molecules of NADH formed in the citric acid cycle; each yields 2.5 molecules of ATP + 15
+ 30
net yield per molecule of glucose
Source: The ATP yield of oxidative phosphorylation is based on values given in P. C. Hinkle, M. A. Kumar, A. Resetar, and D. L. Harris,
Biochemistry 30(1991):3576.
Note: The current value of 30 molecules of ATP per molecule of glucose supersedes the earlier one of 36 molecules of ATP. The stoichiometries
of proton pumping, ATP synthesis, and metabolite transport should be regarded as estimates. About two more molecules of ATP are formed per
molecule of glucose oxidized when the malate-aspartate shuttle rather than the glycerol 3-phosphate shuttle is used.
Adaptación al frío por proteína desacoplante
UCP-1
+
NE
Rβ Ac. Grasos
TG
cAMP PKA
H+
Bajo pH
Alto pH
Generación de radicales de oxígeno asociado al transporte de electrones
Neuropatía óptica
MELAS ( encefalopatía mitocondrial con acidosis láctica)
Mecanismos defensivos: